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SOD1 integrates signals from oxygen and glucose to repress respiration.

Cu/Zn superoxide dismutase (SOD1) is an abundant enzyme that has been best studied as a regulator of antioxidant defense. Using the yeast Saccharomyces cerevisiae, we report that SOD1 transmits signals from oxygen and glucose to repress respiration. The mechanism involves SOD1-mediated stabilization of two casein kinase 1-gamma (CK1γ) homologs, Yck1p and Yck2p, required for respiratory repression. SOD1 binds a C-terminal degron we identified in Yck1p/Yck2p and promotes kinase stability by catalyzing superoxide conversion to peroxide. The effects of SOD1 on CK1γ stability are also observed with mammalian SOD1 and CK1γ and in a human cell line. Therefore, in a single circuit, oxygen, glucose, and reactive oxygen can repress respiration through SOD1/CK1γ signaling. Our data therefore may provide mechanistic insight into how rapidly proliferating cells and many cancers accomplish glucose-mediated repression of respiration in favor of aerobic glycolysis.

Pubmed ID: 23332757


  • Reddi AR
  • Culotta VC



Publication Data

January 17, 2013

Associated Grants

  • Agency: NIGMS NIH HHS, Id: F32 GM 093550
  • Agency: NIGMS NIH HHS, Id: F32 GM093550
  • Agency: NIGMS NIH HHS, Id: GM50016
  • Agency: NIEHS NIH HHS, Id: P30 ES003819
  • Agency: NIGMS NIH HHS, Id: R37 GM050016

Mesh Terms

  • Amino Acid Sequence
  • Casein Kinase I
  • Cell Line
  • Glucose
  • Glycolysis
  • Humans
  • Hydrogen Peroxide
  • Molecular Sequence Data
  • Oxygen
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
  • Superoxide Dismutase
  • Superoxides